SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

D4ZVW7

- D4ZVW7_ARTPN

UniProt

D4ZVW7 - D4ZVW7_ARTPN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Ribulose bisphosphate carboxylase large chain
Gene
cbbL, rbcL, NIES39_K02850
Organism
Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina platensis)
Status
Unreviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site By similarity.UniRule annotation

Catalytic activityi

2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

Cofactori

Binds 1 magnesium ion per subunit By similarity.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei124 – 1241Substrate; in homodimeric partner By similarityUniRule annotation
Binding sitei174 – 1741Substrate By similarityUniRule annotation
Active sitei176 – 1761Proton acceptor By similarityUniRule annotation
Binding sitei178 – 1781Substrate By similarityUniRule annotation
Metal bindingi202 – 2021Magnesium; via carbamate group By similarityUniRule annotation
Metal bindingi204 – 2041Magnesium By similarityUniRule annotation
Metal bindingi205 – 2051Magnesium By similarityUniRule annotation
Active sitei295 – 2951Proton acceptor By similarityUniRule annotation
Binding sitei296 – 2961Substrate By similarityUniRule annotation
Binding sitei328 – 3281Substrate By similarityUniRule annotation
Sitei335 – 3351Transition state stabilizer By similarityUniRule annotation
Binding sitei380 – 3801Substrate By similarityUniRule annotation

GO - Molecular functioni

  1. magnesium ion binding Source: UniProtKB-HAMAP
  2. monooxygenase activity Source: UniProtKB-KW
  3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. photorespiration Source: UniProtKB-KW
  2. reductive pentose-phosphate cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

Keywords - Biological processi

Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation

Keywords - Ligandi

MagnesiumUniRule annotation, Metal-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
Short name:
RuBisCO large subunitUniRule annotation
Gene namesi
Name:cbbLUniRule annotation
Synonyms:rbcLUniRule annotation
ORF Names:NIES39_K02850Imported
OrganismiArthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina platensis)Imported
Taxonomic identifieri696747 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesArthrospira
ProteomesiUP000006803: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-carboxylysine By similarityUniRule annotation
Disulfide bondi248 – 248Interchain; in linked form By similarityUniRule annotation

Post-translational modificationi

The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover By similarity.UniRule annotation

Keywords - PTMi

Disulfide bondUniRule annotation

Interactioni

Subunit structurei

Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliD4ZVW7.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

KOiK01601.

Family and domain databases

Gene3Di3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPiMF_01338. RuBisCO_L_type1.
InterProiIPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view]
PfamiPF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view]
SUPFAMiSSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D4ZVW7-1 [UniParc]FASTAAdd to Basket

« Hide

MSYSQTQTKS KAGYQAGVKD YKLTYYTPDY TPKDTDILAA FRVSPQPGVP    50
PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYHIEP VPGEDNQFFC 100
FVAYPLDLFE EGSVTNMLTS IVGNVFGFKA LRGLRLEDMR IPIAYLKTFQ 150
GPPHGITVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
TKDDENINSQ PFMRWRDRFL FVQEAIEKAQ AETNEIKGHY LNVTAPTCEE 250
MMKRAEFAKE IGTPIIMHDF FTAGFTANTT LARWCRDNGL LLHIHRAMHA 300
VVDRQRNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM 350
REDHIEEDRS RGIFFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC 400
LQFGGGTLGH PWGNAPGATA NRVALEACIQ ARNEGRNLFR EGGDVIREAC 450
KWSPELAVAC ELWKEIKFEF EAMDTL 476
Length:476
Mass (Da):53,280
Last modified:June 15, 2010 - v1
Checksum:iBFC00F25F64B695A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011615 Genomic DNA. Translation: BAI91932.1.
RefSeqiWP_006620100.1. NC_016640.1.
YP_005070470.1. NC_016640.1.

Genome annotation databases

EnsemblBacteriaiBAI91932; BAI91932; NIES39_K02850.
GeneIDi15167013.
KEGGiarp:NIES39_K02850.
PATRICi42721513. VBIArtPla153080_1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP011615 Genomic DNA. Translation: BAI91932.1 .
RefSeqi WP_006620100.1. NC_016640.1.
YP_005070470.1. NC_016640.1.

3D structure databases

ProteinModelPortali D4ZVW7.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAI91932 ; BAI91932 ; NIES39_K02850 .
GeneIDi 15167013.
KEGGi arp:NIES39_K02850.
PATRICi 42721513. VBIArtPla153080_1977.

Phylogenomic databases

KOi K01601.

Family and domain databases

Gene3Di 3.20.20.110. 1 hit.
3.30.70.150. 1 hit.
HAMAPi MF_01338. RuBisCO_L_type1.
InterProi IPR020878. RuBisCo_large_chain_AS.
IPR020888. RuBisCO_lsu.
IPR000685. RuBisCO_lsu_C.
IPR017443. RuBisCO_lsu_fd_N.
IPR017444. RuBisCO_lsu_N.
[Graphical view ]
Pfami PF00016. RuBisCO_large. 1 hit.
PF02788. RuBisCO_large_N. 1 hit.
[Graphical view ]
SUPFAMi SSF51649. SSF51649. 1 hit.
SSF54966. SSF54966. 1 hit.
PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NIES-39 / IAM M-135.

Entry informationi

Entry nameiD4ZVW7_ARTPN
AccessioniPrimary (citable) accession number: D4ZVW7
Entry historyi
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: September 3, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Miscellaneous

The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel" By similarity.UniRule annotation

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

Similar proteinsi